title: Position of the lacZX90 mutation and hybridization between complete and incomplete beta-galactosidase.
abstract: The position of the termination codon in lacZX90 was determined by isolation of a lac+ revertant. Lysine was found to replace tyrosine at position 1,012 of beta-galactosidase, indicating that X90 protein lacked the carboxyl-terminal 10 residues. A heat- and urea-sensitive hybrid enzyme was formed in vivo when supC, which supplies tyrosine to the position in the polypeptide corresponding to the nonsense codon, was used to suppress lacZX90. This result shows that suppression that adds back the original amino acid may not lead to the production of the wild-type enzyme if the latter is multimeric, because incomplete chains can be incorporated into the oligomer.
mesh_terms: D000595:Amino Acid Sequence; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics; D005696:Galactosidases / Q000235:genetics*; D006358:Hot Temperature; D009154:Mutation; D055503:Protein Multimerization; D013489:Suppression, Genetic; D014508:Urea / Q000494:pharmacology; D001616:beta-Galactosidase / Q000235:genetics*
chemical_list: D014508:Urea; D005696:Galactosidases; D001616:beta-Galactosidase